|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05632 |
PRK05632 |
phosphate acetyltransferase; Reviewed |
1-698 |
0e+00 |
|
phosphate acetyltransferase; Reviewed
Pssm-ID: 235537 [Multi-domain] Cd Length: 684 Bit Score: 1166.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 1 MHTFFIAPTGFGVGLTSISLGLLRALERAGLKVGFFKPIAQLhpgdlgpersselvarthgldtpkPLPLAQVERMLGDG 80
Cdd:PRK05632 2 SRSIYLAPTGTGVGLTSVSLGLMRALERKGVKVGFFKPIAQP------------------------PLTMSEVEALLASG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 81 QLDELLEEIISLYQRAAADKDVVIVEGMVPTRHASYAARVNFHLAKSLDAEVILVSAPENETLTELTDRIEIQAQLFGGP 160
Cdd:PRK05632 58 QLDELLEEIVARYHALAKDCDVVLVEGLDPTRKHPFEFSLNAEIAKNLGAEVVLVSSGGNDTPEELAERIELAASSFGGA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 161 RDPKVLGVILNKVRGEADAANA-----EDGVADFARRLTEHSPLLR-DDFRLIGCIPWQDELNAARTRDIADLLSARVIN 234
Cdd:PRK05632 138 KNANILGVIINKLNAPVDEQGRtrpdlSEIFDDSSKANVDPSKLFAsSPLPLLGVVPWSPDLIAPRVIDIAKHLGATVLN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 235 AGDYEQRRVQKIVLCARAVPNTVQLLKPGVLVVTPGDRDDIILAASLAAMNGVPLAGLLLCSDFPPDPRIMELCRGALQG 314
Cdd:PRK05632 218 EGDILTRRVKSVTVCARSIPNMLEHLKPGSLVVTPGDRSDVILAALLAAMNGPPIAGLLLTGGYEPDPRIAKLCEGAFET 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 315 GLPVLSVATGSYDTATNLNRMNKEIPVDDRERAERVTEFVAGHID-FEWLKQRCGT-PRELRLSPPAFRYQVVQRAQKAG 392
Cdd:PRK05632 298 GLPVLSVDTNTYQTALRLQSFNGEVPVDDHERIETVLELVASHVDtDELLERLTATsERSRRLSPPAFRYQLTERARAAK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 393 KRIVLPEGSEPRTVQAAAICQARGIARCVLLAKPEEVQAVAQAQGIVLPEGLEIIDPDLVRQRYVEPMVELRKGKGLNAP 472
Cdd:PRK05632 378 KRIVLPEGDEPRTLKAAAICLERGIADCVLLGNPEEIRRVAAAQGVDLPAGIEIIDPSEVRERYVAPLVELRKHKGMTEE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 473 MAEQQLEDSVVLATMMLALDEVDGLVSGAIHTTASTIRPALQLIKTAPGYNLVSSVFFMLLPDQVLVYGDCAVNPDPSAS 552
Cdd:PRK05632 458 VAREQLEDNVYFGTMMLALGEVDGLVSGAVHTTANTIRPALQLIKTAPGSSLVSSVFFMLLPDQVLVYGDCAVNPDPTAE 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 553 DLAEIAVQSAASAQAFGIPARVAMISYSTGDSGSGVDVDKVREATRLAREQRPDLLIDGPLQYDAAAIASVGRQKAPNSP 632
Cdd:PRK05632 538 QLAEIAIQSADSAAAFGIEPRVAMLSYSTGTSGSGADVEKVREATRLARERRPDLLIDGPLQYDAAVDPSVARSKAPNSP 617
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596032 633 VAGQATVFIFPDLNTGNTTYKAVQRSADCVSVGPMLQGLRKPVNDLSRGALVEDIVYTIALTAIQA 698
Cdd:PRK05632 618 VAGRATVFIFPDLNTGNTTYKAVQRSAGAVSIGPMLQGLRKPVNDLSRGALVDDIVNTIAITAIQA 683
|
|
| PtaN |
COG0857 |
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only]; |
1-702 |
0e+00 |
|
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
Pssm-ID: 440618 [Multi-domain] Cd Length: 697 Bit Score: 795.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 1 MHTFFIAPTGFGVGLTSISLGLLRALERAGLKVGFFKPIAQLHPGDLGPERSSELVARTHGLD----TPKPLPLAQVERM 76
Cdd:COG0857 2 MKSIYIASTEPGSGKTSVALGLARALQRKGLRVGYFKPIGQSLVGGGERDEDVELIREHLGLDlpyeDASPVTLDEVETL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 77 LGDGQLDELLEEIISLYQRAAADKDVVIVEGMVPTR-HASYAARVNFHLAKSLDAEVILVSAPENETLTELTDRIEIQAQ 155
Cdd:COG0857 82 LAEGDPDELLERIVERYEALAAECDVVLVEGSDPTGvGSPFELSLNARIAKNLGAPVLLVASGGGRTPEELVDALLLAAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 156 LFGGpRDPKVLGVILNKVRGEADaanaeDGVADFARRLtehspLLRDDFRLIGCIPWQDELNAARTRDIADLLSARVINA 235
Cdd:COG0857 162 EFRG-EGARVLGVIINRVPPEKL-----EEVREALRPF-----LEGSGIPVLGVIPENPELAAPTVRDLAEALGAEVLNG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 236 GDYEQRRVQKIVLCARAVPNTVQLLKPGVLVVTPGDRDDIILAASLAAMNGVP-LAGLLLCSDFPPDPRIMELCRGALQG 314
Cdd:COG0857 231 GELLDRRVESVVVGAMSVPNALERLREGALVITPGDRSDILLAALLAALSGTPsIAGLILTGGLPPDPAVLRLAEGLGQT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 315 gLPVLSVATGSYDTATNLNRMNKEIPVDDRERAERVTEFVAGHIDFEWLKQRCGTPRElRLSPPAFRYQVVQRAQKAGKR 394
Cdd:COG0857 311 -LPILSVELDTYTTAERLERVRGRIRADDPRKIELALELFAEHVDVDWLLSRLGLPRS-RLSPPAFFYYLLERAARAAKR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 395 IVLPEGSEPRTVQAAAICQARGIARCVLLAKPEEVQAVAQAQGIVLPEGLEIIDPDLVRQRYVEPMVELRKGKGLNAPMA 474
Cdd:COG0857 389 IVLPEGGEDRRILAAAICLLRRIAACVLLGGPEEIIRVAAAQGGLLLDGIEIIDPPDSRLRYVAAEVYLRRRKKKGVTVA 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 475 EQQLEDSVVLATMMLALDEVDGLVSGAIHTTASTIRPALQLIKTAPGYNLVSSVFFMLLPDQVLVYGDCAVNPDPSASDL 554
Cdd:COG0857 469 AAQLEDDVVLYTGMMMVHEGDGLGMGSGATTTTTTTIPPQLIITKTGPGVVSSSSFFLMLLQVVVVGDCACAPNPPPEEL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 555 AEIAVQSAASAQAFGIPARVAMISYSTGDSGSGVDVDKVREATRLAREQRPDLLIDGPLQYDAAAIASVGRQKAPNSPVA 634
Cdd:COG0857 549 ALAAIISSSSAAAAGFGPEPAMISLSSSTSGSGGGVDVVKVATATALVRRRDLLLDGPGPYQAAAAADVVVAKAKPSPVA 628
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596032 635 GQATVFIFPDLNTGNTTYKAVQRSADCVSVGPMLQGLRKPVNDLSRGALVEDIVYTIALTAIQADAQA 702
Cdd:COG0857 629 GAAAAFVFPFLDTNNTNNTAKARQASAGAVAPGPQGLGLPVNDLDLSRGVVDIDITIALTIIAAQQQA 696
|
|
| pta |
TIGR00651 |
phosphate acetyltransferase; Alternate name: phosphotransacetylase Model contains a gene from ... |
395-695 |
6.43e-147 |
|
phosphate acetyltransferase; Alternate name: phosphotransacetylase Model contains a gene from E.coli coding for ethanolamine utilization protein (euti) and also contains similarity to malate oxidoreductases [Central intermediary metabolism, Other, Energy metabolism, Fermentation]
Pssm-ID: 273196 [Multi-domain] Cd Length: 303 Bit Score: 429.94 E-value: 6.43e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 395 IVLPEGSEPRTVQAAAICQARGIARCVLLAKPEEVQAVAQAQGIVLpEGLEIIDPDLV--RQRYVEPMVELRKGKGLNAP 472
Cdd:TIGR00651 1 IVFPEGWEPRVLKAAALLAERGIATPVVLGNPEEIQPKAAGCNLDL-GHVVIIDPDVSpdRESYAERYVELRKHKGMTEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 473 MAEQQLEDSVVLATMMLALDEVDGLVSGAIHTTASTIRPALQLIKTAPGYNLVSSVFFMLLPDQVLVYGDCAVNPDPSAS 552
Cdd:TIGR00651 80 QARKQLRDESYFATMMVALGEADGLVSGAVHTTADTLRPALQIIKTLPGVKIVSSVFIMDLGEEVLVFADCAVNPDPNAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 553 DLAEIAVQSAASAQAFG-IPARVAMISYSTGDSGSGVDVDKVREATRLAREQRPDLLIDGPLQYDAAAIASVGRQKAPNS 631
Cdd:TIGR00651 160 QLAEIAIQSANSAKSFGeIEPKVALLSYSTKGSGKGEEVEKVREATRIAKEKRPDLTIDGELQFDAAFVEKVAEKKAPNS 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596032 632 PVAGQATVFIFPDLNTGNTTYKAVQRSADCVSVGPMLQGLRKPVNDLSRGALVEDIVYTIALTA 695
Cdd:TIGR00651 240 PVAGSANVFVFPDLDAGNIGYKIVQRLGDAEAIGPILQGLNKPVNDLSRGCSVEDIVNTGAITA 303
|
|
| PTA_PTB |
pfam01515 |
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase ... |
380-695 |
2.29e-135 |
|
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase and phosphate butaryltransferase. These enzymes catalyze the transfer of an acetyl or butaryl group to orthophosphate.
Pssm-ID: 396207 [Multi-domain] Cd Length: 318 Bit Score: 400.92 E-value: 2.29e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 380 FRYQVVQRAQKAGKRIVLPEGSEPRTVQAAAICQARGIARCVLLAKPEEVQAVAQAQGIVLpEGLEIIDP--DLVRQRYV 457
Cdd:pfam01515 1 FLERIFERAKKAKKRIVFPEGEDERVLKAAQKLLQQGIADPILIGDEIEIKAKALGLDLDL-DGIEIVDPetSPRLEEYA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 458 EPMVELRKGKGLNAPMAEQQLEDSVVLATMMLALDEVDGLVSGAIHTTASTIRPALQLIKTAPGYNLVSSVFFMLLPDQV 537
Cdd:pfam01515 80 DFYYELRKRKGMTPEIAREIVRDPNYFAAMLVKLGEADGMVSGAVNTTADTLRPALQIIGTKPGVKTVSSVFIMLLPDGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 538 LVYGDCAVNPDPSASDLAEIAVQSAASAQAFGIPA-RVAMISYSTGDSGSGVDVDKVREATRLAREQRPDLLIDGPLQYD 616
Cdd:pfam01515 160 LFFADCAVNPNPTAEELAEIALMSAKTAKRFGIIEpRVALLSYSTFGSGKGEDVEKVREATKIVRERAPDLVVDGELQFD 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596032 617 AAAIASVGRQKAPNSPVAGQATVFIFPDLNTGNTTYKAVQRSADCVSVGPMLQGLRKPVNDLSRGALVEDIVYTIALTA 695
Cdd:pfam01515 240 AALVEEVAAQKAPDSPVAGKANVFVFPDLEAGNIGYKIAQRLGGAEAIGPILQGLAKPVNDLSRGASVEDIVNTAAITA 318
|
|
| DTBS |
cd03109 |
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ... |
2-196 |
4.99e-37 |
|
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors.
Pssm-ID: 349763 [Multi-domain] Cd Length: 189 Bit Score: 136.93 E-value: 4.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 2 HTFFIAPTGFGVGLTSISLGLLRALERAGLKVGFFKPIAQLHPgDLGPERSSELVARTHGLDTPK-------PLPLAQVE 74
Cdd:cd03109 1 KTLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPVQTGCP-GLEDSDAELLRKLAGLLLDLElinpyrfEAPLSPHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 75 RMLGDGQlDELLEEIISLYQRAAADKDVVIVEGMVPTRHASYAARVNFHLAKSLDAEVILVSAPENETLTELTDRIEIQA 154
Cdd:cd03109 80 AAELEGR-DIDLEEIVRALEELAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGTINHTLLTLEALK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15596032 155 QlfggpRDPKVLGVILNKVRGEADAanaedgVADFARRLTEH 196
Cdd:cd03109 159 S-----RGLDVAGVVLNGIPPEPEA------EADNAETLKEL 189
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05632 |
PRK05632 |
phosphate acetyltransferase; Reviewed |
1-698 |
0e+00 |
|
phosphate acetyltransferase; Reviewed
Pssm-ID: 235537 [Multi-domain] Cd Length: 684 Bit Score: 1166.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 1 MHTFFIAPTGFGVGLTSISLGLLRALERAGLKVGFFKPIAQLhpgdlgpersselvarthgldtpkPLPLAQVERMLGDG 80
Cdd:PRK05632 2 SRSIYLAPTGTGVGLTSVSLGLMRALERKGVKVGFFKPIAQP------------------------PLTMSEVEALLASG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 81 QLDELLEEIISLYQRAAADKDVVIVEGMVPTRHASYAARVNFHLAKSLDAEVILVSAPENETLTELTDRIEIQAQLFGGP 160
Cdd:PRK05632 58 QLDELLEEIVARYHALAKDCDVVLVEGLDPTRKHPFEFSLNAEIAKNLGAEVVLVSSGGNDTPEELAERIELAASSFGGA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 161 RDPKVLGVILNKVRGEADAANA-----EDGVADFARRLTEHSPLLR-DDFRLIGCIPWQDELNAARTRDIADLLSARVIN 234
Cdd:PRK05632 138 KNANILGVIINKLNAPVDEQGRtrpdlSEIFDDSSKANVDPSKLFAsSPLPLLGVVPWSPDLIAPRVIDIAKHLGATVLN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 235 AGDYEQRRVQKIVLCARAVPNTVQLLKPGVLVVTPGDRDDIILAASLAAMNGVPLAGLLLCSDFPPDPRIMELCRGALQG 314
Cdd:PRK05632 218 EGDILTRRVKSVTVCARSIPNMLEHLKPGSLVVTPGDRSDVILAALLAAMNGPPIAGLLLTGGYEPDPRIAKLCEGAFET 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 315 GLPVLSVATGSYDTATNLNRMNKEIPVDDRERAERVTEFVAGHID-FEWLKQRCGT-PRELRLSPPAFRYQVVQRAQKAG 392
Cdd:PRK05632 298 GLPVLSVDTNTYQTALRLQSFNGEVPVDDHERIETVLELVASHVDtDELLERLTATsERSRRLSPPAFRYQLTERARAAK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 393 KRIVLPEGSEPRTVQAAAICQARGIARCVLLAKPEEVQAVAQAQGIVLPEGLEIIDPDLVRQRYVEPMVELRKGKGLNAP 472
Cdd:PRK05632 378 KRIVLPEGDEPRTLKAAAICLERGIADCVLLGNPEEIRRVAAAQGVDLPAGIEIIDPSEVRERYVAPLVELRKHKGMTEE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 473 MAEQQLEDSVVLATMMLALDEVDGLVSGAIHTTASTIRPALQLIKTAPGYNLVSSVFFMLLPDQVLVYGDCAVNPDPSAS 552
Cdd:PRK05632 458 VAREQLEDNVYFGTMMLALGEVDGLVSGAVHTTANTIRPALQLIKTAPGSSLVSSVFFMLLPDQVLVYGDCAVNPDPTAE 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 553 DLAEIAVQSAASAQAFGIPARVAMISYSTGDSGSGVDVDKVREATRLAREQRPDLLIDGPLQYDAAAIASVGRQKAPNSP 632
Cdd:PRK05632 538 QLAEIAIQSADSAAAFGIEPRVAMLSYSTGTSGSGADVEKVREATRLARERRPDLLIDGPLQYDAAVDPSVARSKAPNSP 617
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596032 633 VAGQATVFIFPDLNTGNTTYKAVQRSADCVSVGPMLQGLRKPVNDLSRGALVEDIVYTIALTAIQA 698
Cdd:PRK05632 618 VAGRATVFIFPDLNTGNTTYKAVQRSAGAVSIGPMLQGLRKPVNDLSRGALVDDIVNTIAITAIQA 683
|
|
| PtaN |
COG0857 |
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only]; |
1-702 |
0e+00 |
|
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
Pssm-ID: 440618 [Multi-domain] Cd Length: 697 Bit Score: 795.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 1 MHTFFIAPTGFGVGLTSISLGLLRALERAGLKVGFFKPIAQLHPGDLGPERSSELVARTHGLD----TPKPLPLAQVERM 76
Cdd:COG0857 2 MKSIYIASTEPGSGKTSVALGLARALQRKGLRVGYFKPIGQSLVGGGERDEDVELIREHLGLDlpyeDASPVTLDEVETL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 77 LGDGQLDELLEEIISLYQRAAADKDVVIVEGMVPTR-HASYAARVNFHLAKSLDAEVILVSAPENETLTELTDRIEIQAQ 155
Cdd:COG0857 82 LAEGDPDELLERIVERYEALAAECDVVLVEGSDPTGvGSPFELSLNARIAKNLGAPVLLVASGGGRTPEELVDALLLAAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 156 LFGGpRDPKVLGVILNKVRGEADaanaeDGVADFARRLtehspLLRDDFRLIGCIPWQDELNAARTRDIADLLSARVINA 235
Cdd:COG0857 162 EFRG-EGARVLGVIINRVPPEKL-----EEVREALRPF-----LEGSGIPVLGVIPENPELAAPTVRDLAEALGAEVLNG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 236 GDYEQRRVQKIVLCARAVPNTVQLLKPGVLVVTPGDRDDIILAASLAAMNGVP-LAGLLLCSDFPPDPRIMELCRGALQG 314
Cdd:COG0857 231 GELLDRRVESVVVGAMSVPNALERLREGALVITPGDRSDILLAALLAALSGTPsIAGLILTGGLPPDPAVLRLAEGLGQT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 315 gLPVLSVATGSYDTATNLNRMNKEIPVDDRERAERVTEFVAGHIDFEWLKQRCGTPRElRLSPPAFRYQVVQRAQKAGKR 394
Cdd:COG0857 311 -LPILSVELDTYTTAERLERVRGRIRADDPRKIELALELFAEHVDVDWLLSRLGLPRS-RLSPPAFFYYLLERAARAAKR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 395 IVLPEGSEPRTVQAAAICQARGIARCVLLAKPEEVQAVAQAQGIVLPEGLEIIDPDLVRQRYVEPMVELRKGKGLNAPMA 474
Cdd:COG0857 389 IVLPEGGEDRRILAAAICLLRRIAACVLLGGPEEIIRVAAAQGGLLLDGIEIIDPPDSRLRYVAAEVYLRRRKKKGVTVA 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 475 EQQLEDSVVLATMMLALDEVDGLVSGAIHTTASTIRPALQLIKTAPGYNLVSSVFFMLLPDQVLVYGDCAVNPDPSASDL 554
Cdd:COG0857 469 AAQLEDDVVLYTGMMMVHEGDGLGMGSGATTTTTTTIPPQLIITKTGPGVVSSSSFFLMLLQVVVVGDCACAPNPPPEEL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 555 AEIAVQSAASAQAFGIPARVAMISYSTGDSGSGVDVDKVREATRLAREQRPDLLIDGPLQYDAAAIASVGRQKAPNSPVA 634
Cdd:COG0857 549 ALAAIISSSSAAAAGFGPEPAMISLSSSTSGSGGGVDVVKVATATALVRRRDLLLDGPGPYQAAAAADVVVAKAKPSPVA 628
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596032 635 GQATVFIFPDLNTGNTTYKAVQRSADCVSVGPMLQGLRKPVNDLSRGALVEDIVYTIALTAIQADAQA 702
Cdd:COG0857 629 GAAAAFVFPFLDTNNTNNTAKARQASAGAVAPGPQGLGLPVNDLDLSRGVVDIDITIALTIIAAQQQA 696
|
|
| Pta |
COG0280 |
Phosphotransacetylase (includes Pta, EutD and phosphobutyryltransferase) [Energy production ... |
379-697 |
4.48e-150 |
|
Phosphotransacetylase (includes Pta, EutD and phosphobutyryltransferase) [Energy production and conversion];
Pssm-ID: 440049 [Multi-domain] Cd Length: 320 Bit Score: 438.73 E-value: 4.48e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 379 AFRYQVVQRAQKAGKRIVLPEGSEPRTVQAAAICQARGIARCVLLAKPEEVQAVAQAQGIVLpEGLEIIDP--DLVRQRY 456
Cdd:COG0280 1 KFFRPLIERAKAAPKRIVFAEGEDERVLRAAQEALDEGLAEPILVGRPEKIEARAEELGLDL-SGFEIIDPedSPRYEEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 457 VEPMVELRKGKGLNAPMAEQQLEDSVVLATMMLALDEVDGLVSGAIHTTASTIRPALQLIKTAPGYNLVSSVFFMLLPDQ 536
Cdd:COG0280 80 AEAYYELRKRKGVTPEEARELVRDAAYFAAMMVRLGEADGLVKGAVGTTADLLRPVLQIIGLRPGVKRVSHVFLMELPDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 537 VLVYGDCAVNPDPSASDLAEIAVQSAASAQAFGIPARVAMISYSTGDSGSGVDVDKVREATRLAREQRPDLLIDGPLQYD 616
Cdd:COG0280 160 LLFITDTAVNIDPTAEQLADIAINAADTARAFGIEPKVALLSASEFGSPKGPSTDKVREATKMARGQIPDLEVDGELQFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 617 AAAIASVGRQKAPNSPVAGQATVFIFPDLNTGNTTYKAVQRSADCVSVGPMLQGLRKPVNDLSRGALVEDIVYTIALTAI 696
Cdd:COG0280 240 AALSPEAAKRKGPDSPVAGDANVLVFPDLEAGNILYKLLQRLAGAEAIGPILLGLAKPVHLLSRGDSVRDIVNSIALAAV 319
|
.
gi 15596032 697 Q 697
Cdd:COG0280 320 Q 320
|
|
| pta |
TIGR00651 |
phosphate acetyltransferase; Alternate name: phosphotransacetylase Model contains a gene from ... |
395-695 |
6.43e-147 |
|
phosphate acetyltransferase; Alternate name: phosphotransacetylase Model contains a gene from E.coli coding for ethanolamine utilization protein (euti) and also contains similarity to malate oxidoreductases [Central intermediary metabolism, Other, Energy metabolism, Fermentation]
Pssm-ID: 273196 [Multi-domain] Cd Length: 303 Bit Score: 429.94 E-value: 6.43e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 395 IVLPEGSEPRTVQAAAICQARGIARCVLLAKPEEVQAVAQAQGIVLpEGLEIIDPDLV--RQRYVEPMVELRKGKGLNAP 472
Cdd:TIGR00651 1 IVFPEGWEPRVLKAAALLAERGIATPVVLGNPEEIQPKAAGCNLDL-GHVVIIDPDVSpdRESYAERYVELRKHKGMTEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 473 MAEQQLEDSVVLATMMLALDEVDGLVSGAIHTTASTIRPALQLIKTAPGYNLVSSVFFMLLPDQVLVYGDCAVNPDPSAS 552
Cdd:TIGR00651 80 QARKQLRDESYFATMMVALGEADGLVSGAVHTTADTLRPALQIIKTLPGVKIVSSVFIMDLGEEVLVFADCAVNPDPNAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 553 DLAEIAVQSAASAQAFG-IPARVAMISYSTGDSGSGVDVDKVREATRLAREQRPDLLIDGPLQYDAAAIASVGRQKAPNS 631
Cdd:TIGR00651 160 QLAEIAIQSANSAKSFGeIEPKVALLSYSTKGSGKGEEVEKVREATRIAKEKRPDLTIDGELQFDAAFVEKVAEKKAPNS 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596032 632 PVAGQATVFIFPDLNTGNTTYKAVQRSADCVSVGPMLQGLRKPVNDLSRGALVEDIVYTIALTA 695
Cdd:TIGR00651 240 PVAGSANVFVFPDLDAGNIGYKIVQRLGDAEAIGPILQGLNKPVNDLSRGCSVEDIVNTGAITA 303
|
|
| eutD |
PRK09653 |
phosphotransacetylase; |
383-701 |
3.41e-136 |
|
phosphotransacetylase;
Pssm-ID: 236609 [Multi-domain] Cd Length: 324 Bit Score: 403.07 E-value: 3.41e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 383 QVVQRAQKAGKRIVLPEGSEPRTVQAAAICQARGIARCVLLAKPEEVQAVAQAQGIVLpEGLEIIDP--DLVRQRYVEPM 460
Cdd:PRK09653 6 SLKEKAKGKKKKIVLPEGEDERVLKAAKRLQKEGLVEPILLGNPEEIRAKAKELGLDL-DGVEIIDPetYPLLEEFAEAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 461 VELRKGKGLnAPMAEQQLEDSVVLATMMLALDEVDGLVSGAIHTTASTIRPALQLIKTAPGYNLVSSVFFMLLPDQVLVY 540
Cdd:PRK09653 85 VELRKGKGT-EEDAAELLKDPNYFGTMLVKLGKADGMVSGAIHSTADTLRPALQIIKTKPGVKTVSSVFIMVKGDERYIF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 541 GDCAVNPDPSASDLAEIAVQSAASAQAFGIPARVAMISYSTGDSGSGVDVDKVREATRLAREQRPDLLIDGPLQYDAAAI 620
Cdd:PRK09653 164 ADCAVNPNPTAEQLAEIAINSAETAKAFGIDPKVAMLSFSTKGSAKGPEVDKVQEATEIAKELAPDLKIDGELQFDAAFV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 621 ASVGRQKAPNSPVAGQATVFIFPDLNTGNTTYKAVQRSADCVSVGPMLQGLRKPVNDLSRGALVEDIVYTIALTAIQADA 700
Cdd:PRK09653 244 PEVAAKKAPGSPVAGKANVFVFPSLEAGNIGYKIAQRLGGFEAVGPILQGLNKPVNDLSRGCSVEDIYNLALITAAQAQG 323
|
.
gi 15596032 701 Q 701
Cdd:PRK09653 324 E 324
|
|
| PTA_PTB |
pfam01515 |
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase ... |
380-695 |
2.29e-135 |
|
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase and phosphate butaryltransferase. These enzymes catalyze the transfer of an acetyl or butaryl group to orthophosphate.
Pssm-ID: 396207 [Multi-domain] Cd Length: 318 Bit Score: 400.92 E-value: 2.29e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 380 FRYQVVQRAQKAGKRIVLPEGSEPRTVQAAAICQARGIARCVLLAKPEEVQAVAQAQGIVLpEGLEIIDP--DLVRQRYV 457
Cdd:pfam01515 1 FLERIFERAKKAKKRIVFPEGEDERVLKAAQKLLQQGIADPILIGDEIEIKAKALGLDLDL-DGIEIVDPetSPRLEEYA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 458 EPMVELRKGKGLNAPMAEQQLEDSVVLATMMLALDEVDGLVSGAIHTTASTIRPALQLIKTAPGYNLVSSVFFMLLPDQV 537
Cdd:pfam01515 80 DFYYELRKRKGMTPEIAREIVRDPNYFAAMLVKLGEADGMVSGAVNTTADTLRPALQIIGTKPGVKTVSSVFIMLLPDGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 538 LVYGDCAVNPDPSASDLAEIAVQSAASAQAFGIPA-RVAMISYSTGDSGSGVDVDKVREATRLAREQRPDLLIDGPLQYD 616
Cdd:pfam01515 160 LFFADCAVNPNPTAEELAEIALMSAKTAKRFGIIEpRVALLSYSTFGSGKGEDVEKVREATKIVRERAPDLVVDGELQFD 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596032 617 AAAIASVGRQKAPNSPVAGQATVFIFPDLNTGNTTYKAVQRSADCVSVGPMLQGLRKPVNDLSRGALVEDIVYTIALTA 695
Cdd:pfam01515 240 AALVEEVAAQKAPDSPVAGKANVFVFPDLEAGNIGYKIAQRLGGAEAIGPILQGLAKPVNDLSRGASVEDIVNTAAITA 318
|
|
| PRK07232 |
PRK07232 |
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed |
383-702 |
3.46e-74 |
|
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
Pssm-ID: 235976 [Multi-domain] Cd Length: 752 Bit Score: 254.63 E-value: 3.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 383 QVVQRAQKAGKRIVLPEGSEPRTVQAAAICQARGIARCVLLAKPEEVQAVAQAQG--IVLPEGLEIIDP--DLVRQRYVE 458
Cdd:PRK07232 430 PIFAKAKKDPKRVVFAEGEEERVLRAAQEVVDEGLAKPILIGRPEVIEARIKKLGldLKAGVDFEIVNPedDPRYEEYWQ 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 459 PMVELRKGKGLNAPMAEQQLE-DSVVLATMMLALDEVDGLVSGAIHTTASTIRPALQLIKTAPGYNLVSSVFFMLLPDQV 537
Cdd:PRK07232 510 YYYELLQRKGVTPEDARRLVRrDRTVIGAMMVARGDADAMICGLTGRYHEHLRPVRQVIGLRPGVHTAAAMNALLLKGGN 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 538 LVYGDCAVNPDPSASDLAEIAVQSAASAQAFGIPARVAMISYSTGDSGSGVDVDKVREATRLAREQRPDLLIDGPLQYDA 617
Cdd:PRK07232 590 LFIADTYVNEDPTAEELAEIALMAAEEVRRFGIEPRVALLSHSNFGSSDSPSARKMREAVELLRERAPDLEVDGEMHGDA 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 618 AAIASVGRQKAPNSPVAGQATVFIFPDLNTGNTTYKAVQRSADCVSVGPMLQGLRKPVNDLSRGALVEDIVYTIALTAiq 697
Cdd:PRK07232 670 ALNEEIRKDLYPFSRLKGPANVLVMPNLEAANISYNLLKELGGGVTIGPILLGMAKPVHILTPSATVRRIVNMTALAV-- 747
|
....*
gi 15596032 698 ADAQA 702
Cdd:PRK07232 748 VDAQT 752
|
|
| PRK12862 |
PRK12862 |
malic enzyme; Reviewed |
384-702 |
9.84e-56 |
|
malic enzyme; Reviewed
Pssm-ID: 183799 [Multi-domain] Cd Length: 763 Bit Score: 203.58 E-value: 9.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 384 VVQRAQKAGKRIVLPEGSEPRTVQAAAICQARGIARCVLLAKPEEVQAVAQAQGIVLPEG--LEIIDP--DLVRQRYVEP 459
Cdd:PRK12862 439 VFAAAKAAPKRVVFAEGEDERVLRAAQVVVDEGLAKPILIGRPAVIEARIERAGLRLRPGvdFEIVNPedDPRYRDYWDT 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 460 MVELRKGKGLNAPMAEQQL-EDSVVLATMMLALDEVDGLVSGAIHTTASTIRPALQLIKTAPGYNLVSSVFFMLLPDQVL 538
Cdd:PRK12862 519 YHALMGRKGVTPEMARREVrRRTTLIGAMMVKRGEADAMICGTEGRYERHLEFVLQVIGKRPGVRVYAAMSLLILPGRTL 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 539 VYGDCAVNPDPSASDLAEIAVQSAASAQAFGIPARVAMISYSTGDSGSGVDVDKVREATRLAREQRPDLLIDGPLQYDAA 618
Cdd:PRK12862 599 FLADTHVNEDPTAEELAEITILAAEEVRRFGIEPKVALLSHSNFGSSDSPSARKMREALEILRERAPDLEVDGEMHGDAA 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 619 AIASVGRQKAPNSPVAGQATVFIFPDLNTGNTTYKAVQRSA-DCVSVGPMLQGLRKPVNDLSRGALVEDIVYTIALTAIQ 697
Cdd:PRK12862 679 LDEELRDRIFPDSRLEGEANLLVFPNLDAANIAYNLLKTAAgNGLAVGPILLGAAKPVHILTPSATVRRIVNMTALAVAD 758
|
....*
gi 15596032 698 ADAQA 702
Cdd:PRK12862 759 ANAYR 763
|
|
| PRK12861 |
PRK12861 |
malic enzyme; Reviewed |
383-702 |
1.21e-38 |
|
malic enzyme; Reviewed
Pssm-ID: 183798 [Multi-domain] Cd Length: 764 Bit Score: 153.12 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 383 QVVQRAQKAgkRIVLPEGSEPRTVQAAAICQARGIARCVLLAKPEEVQAVAQAQG--IVLPEGLEIIDPDLVRQ--RYVE 458
Cdd:PRK12861 441 QLVRDGGKA--RIVFTEGEDERVLRAVQVIVDEKLARPILVGRPEVLLARIERFGlrLRLGQDVEVTNPEYDERfpQYWT 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 459 PMVELRKGKGLNAPMAEQQLEDSVVL-ATMMLALDEVDGLVSGAIHTTASTIRPALQLIKTAPGYNLVSSVFFMLLPDQV 537
Cdd:PRK12861 519 TYWELRCRDGISKEMARVEMRRRLTLiGAMMVRLGDADGMICGTVGEYHNHLRFVDEVIGRKPGASTYAAMNILLLDQRT 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 538 LVYGDCAVNPDPSASDLAEIAVQSAASAQAFGIPARVAMISYSTGDSGSGVDVDKVREATRLAREQRPDLLIDGPLQYDA 617
Cdd:PRK12861 599 VALVDTHVNDNPDAEQIAEFTIAAARQMEWLNLTPKVALLSRSNFGSGSAASGVKMRRALEIVREQAPDLEADGEMHGDC 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 618 AAIASVGRQKAPNSPVAGQATVFIFPDLNTGNTTYKAVQRSA-DCVSVGPMLQGLRKPVNDLSRGALVEDIVYTIALTAI 696
Cdd:PRK12861 679 ALDEGLRARLLPMSPLKGAANLLVCPNVDAGNIAYNLLKTEAgSNVAVGPFLLGVNAPVNILTSSATVRRIVNMAALTVI 758
|
....*.
gi 15596032 697 QADAQA 702
Cdd:PRK12861 759 EANRNV 764
|
|
| DTBS |
cd03109 |
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ... |
2-196 |
4.99e-37 |
|
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors.
Pssm-ID: 349763 [Multi-domain] Cd Length: 189 Bit Score: 136.93 E-value: 4.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 2 HTFFIAPTGFGVGLTSISLGLLRALERAGLKVGFFKPIAQLHPgDLGPERSSELVARTHGLDTPK-------PLPLAQVE 74
Cdd:cd03109 1 KTLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPVQTGCP-GLEDSDAELLRKLAGLLLDLElinpyrfEAPLSPHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 75 RMLGDGQlDELLEEIISLYQRAAADKDVVIVEGMVPTRHASYAARVNFHLAKSLDAEVILVSAPENETLTELTDRIEIQA 154
Cdd:cd03109 80 AAELEGR-DIDLEEIVRALEELAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGTINHTLLTLEALK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15596032 155 QlfggpRDPKVLGVILNKVRGEADAanaedgVADFARRLTEH 196
Cdd:cd03109 159 S-----RGLDVAGVVLNGIPPEPEA------EADNAETLKEL 189
|
|
| DRTGG |
pfam07085 |
DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated ... |
223-335 |
1.20e-33 |
|
DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated with CBS domains pfam00571, as well as the CbiA domain pfam01656. The function of this domain is unknown. It is named the DRTGG domain after some of the most conserved residues. This domain may be very distantly related to a pair of CBS domains. There are no significant sequence similarities, but its length and association with CBS domains supports this idea (Bateman A, pers. obs.).
Pssm-ID: 429285 [Multi-domain] Cd Length: 105 Bit Score: 124.15 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 223 DIADLLSARVINAGDYEQRRVQKIVLCARAVPNTVQLLKPGVLVVTPGDRDDIILAASLAAmngvpLAGLLLCSDFPPDP 302
Cdd:pfam07085 1 DIARILGAEVLNGGDGLLRRVGKVVVGAMSVENMLKYLRPGDLVITPGDREDIQLAALEAG-----IAGLILTGGFEPSP 75
|
90 100 110
....*....|....*....|....*....|...
gi 15596032 303 RIMELCRGAlqgGLPVLSVATGSYDTATNLNRM 335
Cdd:pfam07085 76 EVLKLAEEL---GLPVLSTPYDTFTTASRINRA 105
|
|
| AAA_26 |
pfam13500 |
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ... |
2-220 |
9.70e-30 |
|
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif.
Pssm-ID: 433259 [Multi-domain] Cd Length: 198 Bit Score: 116.59 E-value: 9.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 2 HTFFIAPTGFGVGLTSISLGLLRALERAGLKVGFFKPIAQLHPGDLGPERSSELVARTHGLDTPKPLPLAQVERMLGDGQ 81
Cdd:pfam13500 1 RTLFVTGTDTGVGKTVVSLGLARALKRRGVKVGYWKPVQTGLVEDGDSELVKRLLGLDQSYEDPEPFRLSAPLSPHLAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 82 LDELLEEIISLYQRAAADKDVVIVEGMVPTRHASYAARVNFHLAKSLDAEVILVSAPENETLteltDRIEIQAQLFgGPR 161
Cdd:pfam13500 81 QEGVTIDLEKIIYELPADADPVVVEGAGGLLVPINEDLLNADIAANLGLPVILVARGGLGTI----NHTLLTLEAL-RQR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15596032 162 DPKVLGVILNKVRGEADAANaedgvadfarrLTEHSPLlrddfRLIGCIPWQDELNAAR 220
Cdd:pfam13500 156 GIPVLGVILNGVPNPENVRT-----------IFAFGGV-----PVLGAVPYLPDLTAPT 198
|
|
| BioD |
COG0132 |
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ... |
1-230 |
1.28e-17 |
|
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439902 [Multi-domain] Cd Length: 222 Bit Score: 82.13 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 1 MHTFFIAPTGFGVGLTSISLGLLRALERAGLKVGFFKPIA--------QLHPGDlgpersSELVARTHGLDTPK------ 66
Cdd:COG0132 1 MKGLFVTGTDTDVGKTVVTAALAAALRAAGLRVGYYKPVQtgceetdgGLRNGD------AELLRRLSGLPLSYelvnpy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 67 --PLPL-----AQVERMlgdgQLDelLEEIISLYQRAAADKDVVIVEG----MVP-TRHASYAarvnfHLAKSLDAEVIL 134
Cdd:COG0132 75 rfEEPLsphlaARLEGV----PID--LDKILAALRALAARYDLVLVEGagglLVPlTEDLTLA-----DLAKALGLPVIL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 135 VSAPE----NETLteLTdrIE-IQAqlfggpRDPKVLGVILNKV--RGEADAANAEDgvadfarrLTEHSPLlrddfRLI 207
Cdd:COG0132 144 VVRARlgtiNHTL--LT--VEaLRA------RGLPLAGIVLNGVppPDLAERDNLET--------LERLTGA-----PVL 200
|
250 260
....*....|....*....|...
gi 15596032 208 GCIPWQDELNAArtrDIADLLSA 230
Cdd:COG0132 201 GVLPYLADLDPE---ALAAYLDL 220
|
|
| PRK05805 |
PRK05805 |
phosphate butyryltransferase; Validated |
401-699 |
1.82e-13 |
|
phosphate butyryltransferase; Validated
Pssm-ID: 180267 Cd Length: 301 Bit Score: 71.66 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 401 SEPRTVQAA---------AICQAR--GIARCVLLAKPEEVQAVAQAQGIVLpEGLEIIDPDLVRQRYVEPmVEL-RKGKg 468
Cdd:PRK05805 15 QPPKTISVAvaqdepvleAVKEAKelGIANAILVGDKEKIKEIAKEIDMDL-EDFEIIDEKDNRKAALKA-VELvSSGK- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 469 lnAPMAEQQLEDSvvlATMMLA-LDEVDGLVSGAIHTTASTIRpalqliktAPGYnlvssvffmllpDQVLVYGDCAVNP 547
Cdd:PRK05805 92 --ADMVMKGLVDT---ANFLRAvLNKEIGLRTGKTMSHVAVFE--------VPKY------------DRLLFLTDAAFNI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 548 DPSASDLAEIAVQSAASAQAFGIPA-RVAMISystgdsgsgvDVDKVR-------EATRLA----REQRPDLLIDGPLQY 615
Cdd:PRK05805 147 APDLKEKIDIINNAVTVAHAIGIENpKVAPIC----------AVEVVNpkmpatlDAALLSkmsdRGQIKGCIVDGPLAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 616 DAAAIASVGRQKAPNSPVAGQATVFIFPDLNTGNTTYKAVQRSADCVSVGpMLQGLRKPVNDLSRGALVEDIVYTIALTA 695
Cdd:PRK05805 217 DNALSEEAAKHKGIDGPVAGNADILLVPNIEAGNVMYKTLTYFADCKNGG-LLVGTSAPVVLTSRADSHETKLNSIALAA 295
|
....
gi 15596032 696 IQAD 699
Cdd:PRK05805 296 LVAA 299
|
|
| CobB_N |
cd05388 |
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase ... |
2-217 |
1.42e-12 |
|
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase (CobB, CbiA). Biosynthesis of cobalamin (vitamin B12) requires more than two dozen different enzymes. CobB catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinic acid, via the formation of a phosphorylated intermediate, using glutamine or ammonia as the nitrogen source. CobB is comprised of two protein domains: the C-terminal glutaminase domain and the N-terminal ATP-binding domain. The glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. It belongs to the triad class of glutamine amidotransferases. This classification is based on the N-terminal domain which catalyzes the ultimate synthesis of the diamide product by using energy from the hydrolysis of ATP and ammonia transferred from the C-terminal domain.
Pssm-ID: 349773 [Multi-domain] Cd Length: 193 Bit Score: 66.86 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 2 HTFFIAPTGFGVGLTSISLGLLRALERAGLKVGFFKpiaqlhpgdLGP--------ERSSElvARTHGLDTpkplplaqv 73
Cdd:cd05388 1 PRIVIAGTSSGSGKTTITLGLMRALARRGLRVQPFK---------VGPdyidpgfhEAATG--RPSRNLDS--------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 74 eRMLGdgqldelLEEIISLYQRAAADKDVVIVE-------GMVPTRHASYAArvnfHLAKSLDAEVILVSAPENETLTel 146
Cdd:cd05388 61 -WMMG-------EDGVRELFARAAGGADVAIIEgvmglydGRDTDSDEGSTA----ELARLLGAPVLLVLDCKGMARS-- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596032 147 tdrieIQAQLFG---GPRDPKVLGVILNKVRGEADAANAEDGVADFARrltehspllrddFRLIGCIPWQDELN 217
Cdd:cd05388 127 -----AAAIVKGykeFDPDLNLAGVILNRVGSPRHAELLKEAIEEYTG------------IPVLGYLPRDDELT 183
|
|
| PRK07742 |
PRK07742 |
phosphate butyryltransferase; Validated |
406-693 |
1.10e-10 |
|
phosphate butyryltransferase; Validated
Pssm-ID: 236086 Cd Length: 299 Bit Score: 63.19 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 406 VQAAAICQARGIArcVLLAKPEEV-QAVAQAqgivlpegleiIDPDLVRQRYV---EPMVELRKGKGLNAP-----MAEQ 476
Cdd:PRK07742 7 IDQAAGQPKKTVA--VAVAEDEEViEAVAKA-----------IELQLARFRLYgnqEKIMGMLQEHGLQTSehieiIHAQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 477 QLEDSVVLATMMLALDEVDGLVSGAIhTTASTIRPALQLIKTAPGYNLVSSVFFMLLP--DQVLVYGDCAVNPDPSASDL 554
Cdd:PRK07742 74 SSAEAAELAVKAVRNGEADVLMKGNV-PTANILKAVLNKEWGLRKGSVLSHVAVFEVPnyDRLIFVTDAAMNIAPDLEQK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 555 AEIAVQSAASAQAFGIPA-RVAMISystgdsgsGVD-VDKVREATRLA--------REQRPDLLIDGPLQYDAAAIASVG 624
Cdd:PRK07742 153 AAIIQNAVEVARAIGIDLpKVAPLA--------AVEvVNPAMQATIDAaaltqmnrRGQIKNCVVDGPLALDNAVSQIAA 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596032 625 RQKAPNSPVAGQATVFIFPDLNTGNTTYKAVQRSADcVSVGPMLQGLRKPVNDLSRGALVEDIVYTIAL 693
Cdd:PRK07742 225 EHKGIVSDVAGKADILLVPTIEAGNVLYKSLVYFAD-AKVGAMIAGAKAPIVLTSRADSAETKLYSLAL 292
|
|
| CobB |
COG1797 |
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ... |
4-216 |
3.29e-10 |
|
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a,c-diamide synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441402 [Multi-domain] Cd Length: 459 Bit Score: 62.82 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 4 FFIAPTGFGVGLTSISLGLLRALERAGLKVGFFK--P--I-AQLHpgdlgperssELVA--RTHGLDTpkplplaqveRM 76
Cdd:COG1797 6 LVIAAPHSGSGKTTVTLGLLAALRRRGLKVQPFKvgPdyIdPGYH----------TLATgrPSRNLDP----------FL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 77 LGDgqldellEEIISLYQRAAADKDVVIVEGM--------VPTRHASYAarvnfHLAKSLDAEVILVSAPENETLTeltd 148
Cdd:COG1797 66 MGE-------EGVRELFARGSAGADIAVIEGVmglydgldGDSGSGSTA-----HLAKLLGAPVVLVVDASGMSRS---- 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596032 149 rieIQAQLFG----GPrDPKVLGVILNKVRGEAdaanaedgvadfarrlteHSPLLRD------DFRLIGCIPWQDEL 216
Cdd:COG1797 130 ---AAALVLGfrafDP-DVRIAGVILNRVGSER------------------HEELLREaiehytGIPVLGALPRDEEL 185
|
|
| PRK01077 |
PRK01077 |
cobyrinate a,c-diamide synthase; |
1-216 |
3.74e-10 |
|
cobyrinate a,c-diamide synthase;
Pssm-ID: 234896 [Multi-domain] Cd Length: 451 Bit Score: 62.84 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 1 MHTFFIAPTGFGVGLTSISLGLLRALERAGLKVGFFKpiaqlhpgdLGP------------ERSSelvartHGLDTpkpl 68
Cdd:PRK01077 3 MPALVIAAPASGSGKTTVTLGLMRALRRRGLRVQPFK---------VGPdyidpayhtaatGRPS------RNLDS---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 69 plaqveRMLGDGQLDElleeiisLYQRAAADKDVVIVEGM--------VPTRHASYAarvnfHLAKSLDAEVILV---SA 137
Cdd:PRK01077 64 ------WMMGEELVRA-------LFARAAQGADIAVIEGVmglfdgagSDPDEGSTA-----DIAKLLGAPVVLVvdaSG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 138 penetlteltdrieiQAQLFG----GPR--DPKVL--GVILNKVRGEAdaanaedgvadfarrlteHSPLLRD-----DF 204
Cdd:PRK01077 126 ---------------MAQSAAalvlGFAtfDPDVRiaGVILNRVGSER------------------HYQLLREalercGI 172
|
250
....*....|..
gi 15596032 205 RLIGCIPWQDEL 216
Cdd:PRK01077 173 PVLGALPRDAAL 184
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
4-219 |
6.46e-09 |
|
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.
Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 56.97 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 4 FFIAPTGFGVGLTSISLGLLRALERAGLKVGFFKPIAQ---LHPGDLGPERSSELVA--------------------RTH 60
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQsnnSSVEGLEGDIAPALQAlaeglkgrvnldpillkeksDEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 61 GLDT-PKPLPLAQVERMLGDGQLDELLEEIIslyQRAAADKDVVIVEGM----VPTRHASYAARvnfHLAKSLDAEVILV 135
Cdd:pfam01656 81 GLDLiPGNIDLEKFEKELLGPRKEERLREAL---EALKEDYDYVIIDGApglgELLRNALIAAD---YVIIPLEPEVILV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 136 SAPENetLTELTDRIEIQAQLFGgprdPKVLGVILNKVRGEADAANAEDGVADFARRLtehspllrddfRLIGCIPWQDE 215
Cdd:pfam01656 155 EDAKR--LGGVIAALVGGYALLG----LKIIGVVLNKVDGDNHGKLLKEALEELLRGL-----------PVLGVIPRDEA 217
|
....
gi 15596032 216 LNAA 219
Cdd:pfam01656 218 VAEA 221
|
|
| bioD |
TIGR00347 |
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ... |
5-171 |
4.08e-08 |
|
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses the reaction (CO2 + 7,8-diaminononanoate + ATP = dethiobiotin + phosphate + ADP). The enzyme binds ATP (see motif in first 12 residues of the SEED alignment) and requires magnesium as a co-factor. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 129447 [Multi-domain] Cd Length: 166 Bit Score: 53.13 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 5 FIAPTGFGVGLTSISLGLLRALERAGLKVGFFKPIA---QLHPGDLGPERSSELVARTHGLDTPKPL--PLAQVERMLGD 79
Cdd:TIGR00347 1 FVTGTDTGVGKTVASSALAAKLKKAGYSVGYYKPVQtgiEKTNSDALLLQNISGTALDWDEVNPYAFalPLSPHIAADQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 80 GQLDElLEEIISLYQRAAADKDVVIVEG----MVPTRH-ASYAarvnfHLAKSLDAEVILVSAPE----NETLteLTDRI 150
Cdd:TIGR00347 81 GRPID-LEELSKHLRTLEQKYDFVLVEGagglCVPITEeYTTA-----DLIKLLQLPVILVVRVKlgtiNHTL--LTVEH 152
|
170 180
....*....|....*....|.
gi 15596032 151 EIQAQLfggprdpKVLGVILN 171
Cdd:TIGR00347 153 ARQTGL-------TLAGVILN 166
|
|
| PRK14869 |
PRK14869 |
putative manganese-dependent inorganic diphosphatase; |
163-342 |
1.31e-06 |
|
putative manganese-dependent inorganic diphosphatase;
Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 51.76 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 163 PKVLGVILNKVRGeadaANAEDGVADFARRLTEHS----PLLRDDFRLIGCI-----------PWQDE-LNAART--RDI 224
Cdd:PRK14869 68 PQVRDLEIDKPVT----VSPDTSLKEAWNLMDENNvktlPVVDEEGKLLGLVslsdlaraymdILDPEiLSKSPTslENI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 225 ADLLSARVINAGDYEQRRVQKIVLCARAVPNTVQLLKPGVLVVTpGDRDDIILAASLAamnGVPLagLLLCSDFPPDPRI 304
Cdd:PRK14869 144 IRTLDGEVLVGAEEDKVEEGKVVVAAMAPESLLERIEEGDIVIV-GDREDIQLAAIEA---GVRL--LIITGGAPVSEDV 217
|
170 180 190
....*....|....*....|....*....|....*...
gi 15596032 305 MELcrgALQGGLPVLSVatgSYDTATNLNRMNKEIPVD 342
Cdd:PRK14869 218 LEL---AKENGVTVIST---PYDTFTTARLINQSIPVS 249
|
|
| PRK08190 |
PRK08190 |
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated |
608-675 |
6.93e-06 |
|
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
Pssm-ID: 236180 [Multi-domain] Cd Length: 466 Bit Score: 49.11 E-value: 6.93e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596032 608 LIDGPLQYDAAAIASVGRQKAPNSPVAGQATVFIFPDLNTGNTTYKAVQRSADCVSVGPMLqGLRKPV 675
Cdd:PRK08190 368 IVDGPLAFDNAISAEAARTKGIVSPVAGQADILVVPDLEAGNMLAKQLTYLAGADAAGIVL-GARVPI 434
|
|
| PRK11890 |
PRK11890 |
phosphate acetyltransferase; Provisional |
525-680 |
3.66e-05 |
|
phosphate acetyltransferase; Provisional
Pssm-ID: 183361 Cd Length: 312 Bit Score: 46.14 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 525 VSSVFFMLLP--DQVLVYGDCAVNPDPSASDLAEIAVQSAASAQAFGIP-ARVAMISystgdsgsGVDV--DKVR---EA 596
Cdd:PRK11890 127 ISHVFVMDVPgyPKPLIITDAAVNIAPTLEDKADIVQNAIDLAHALGFDePRVAILS--------AVETvnPKIPstlDA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 597 TRLA----REQRPDLLIDGPLQYDAAAIASVGRQKAPNSPVAGQATVFIFPDLNTGNTTYKAVQRSADCVSVGPMLqGLR 672
Cdd:PRK11890 199 AALCkmadRGQITGAILDGPLAFDNAISPEAARIKGIVSPVAGDADILVVPDLEAGNMLAKQLTFLAGADAAGIVL-GAR 277
|
....*...
gi 15596032 673 KPVNDLSR 680
Cdd:PRK11890 278 VPIILTSR 285
|
|
| CobQ_N |
cd05389 |
N-terminal domain of cobyric acid synthase; Cobyric acid synthase (CobQ, CbiP) N-terminal ... |
6-178 |
3.32e-04 |
|
N-terminal domain of cobyric acid synthase; Cobyric acid synthase (CobQ, CbiP) N-terminal domain. CobQ plays a role in the cobalamin (vitamin B12) biosynthesis pathway. CobQ catalyzes the ATP-dependent amidation of adenosyl-cobyrinic acid a,c-diamide at carboxylates positions b, d, e, and g to produce cobyric acid using glutamine or ammonia as the nitrogen source. The C-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. Ammonia is translocated via an intramolecular tunnel to the N-terminal domain for the synthesis of cobyric acid.
Pssm-ID: 349774 Cd Length: 223 Bit Score: 42.58 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 6 IAPTGFGVGLTSISLGLLRALERAGLKVGFFKpiAQ-----LHPGDLGPE--RSSELVARTHGLDT----------PKPL 68
Cdd:cd05389 5 VQGTASDVGKSTLVAALCRILKRRGYRVAPFK--AQnmslnSFVTKDGGEigRAQAVQAEAAGVEPsvdmnpvllkPKGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 69 PLAQV---ERMLGD-------GQLDELLEEIISLYQRAAADKDVVIVEGmvptrhASYAAR--------VNFHLAKSLDA 130
Cdd:cd05389 83 FKSQVivmGKPIGDmdareyyEYKGRLAPAVLESLDRLAAEYDLVVIEG------AGSPAEinlrdrdiVNMGMARAADA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15596032 131 EVILVSApenetltelTDRIEIQAQLFGG-----PRDPK-VLGVILNKVRGEAD 178
Cdd:cd05389 157 PVILVAD---------IDRGGVFASLYGTlallpEEERKlVKGVVINKFRGDRS 201
|
|
| PRK00784 |
PRK00784 |
cobyric acid synthase; |
83-217 |
8.43e-03 |
|
cobyric acid synthase;
Pssm-ID: 234838 [Multi-domain] Cd Length: 488 Bit Score: 39.30 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596032 83 DELLEEIISLYQRAAADKDVVIVEGmvptrhA-SYA-----AR--VNFHLAKSLDAEVILVSapenetlteltDrIE--- 151
Cdd:PRK00784 109 PRLLEAVLESLDRLAAEYDVVVVEG------AgSPAeinlrDRdiANMGFAEAADAPVILVA-----------D-IDrgg 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596032 152 IQAQLFG-----GPRDPK-VLGVILNKVRGeaDAANAEDGVadfaRRLTEHS--PLLrddfrliGCIPWQDELN 217
Cdd:PRK00784 171 VFASLVGtlallPPEERArVKGFIINKFRG--DISLLEPGL----DWLEELTgvPVL-------GVLPYLDDLR 231
|
|
| |
